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Q64520

- KGUA_MOUSE

UniProt

Q64520 - KGUA_MOUSE

Protein

Guanylate kinase

Gene

Guk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Essential for recycling GMP and indirectly, cGMP.

    Catalytic activityi

    ATP + GMP = ADP + GDP.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei44 – 4411 Publication
    Active sitei137 – 13711 Publication
    Active sitei148 – 14811 Publication
    Binding sitei171 – 1711ATP
    Binding sitei172 – 1721ATP; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 188ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. guanylate kinase activity Source: UniProtKB

    GO - Biological processi

    1. ATP metabolic process Source: Ensembl
    2. dATP metabolic process Source: Ensembl
    3. dGDP biosynthetic process Source: Ensembl
    4. dGMP metabolic process Source: Ensembl
    5. GDP biosynthetic process Source: Ensembl
    6. GDP-mannose metabolic process Source: Ensembl
    7. glycoprotein transport Source: Ensembl
    8. GMP metabolic process Source: Ensembl
    9. purine nucleotide metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196553. Abacavir metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanylate kinase (EC:2.7.4.8)
    Alternative name(s):
    GMP kinase
    Gene namesi
    Name:Guk1
    Synonyms:Gmk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:95871. Guk1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 198197Guanylate kinasePRO_0000170652Add
    BLAST

    Proteomic databases

    PaxDbiQ64520.
    PRIDEiQ64520.

    PTM databases

    PhosphoSiteiQ64520.

    Expressioni

    Gene expression databases

    ArrayExpressiQ64520.
    BgeeiQ64520.
    CleanExiMM_GUK1.
    GenevestigatoriQ64520.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    IntActiQ64520. 2 interactions.
    MINTiMINT-4099756.

    Structurei

    Secondary structure

    1
    198
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104
    Helixi17 – 2812
    Turni29 – 313
    Beta strandi32 – 343
    Turni49 – 513
    Helixi58 – 6710
    Beta strandi70 – 767
    Beta strandi79 – 846
    Helixi85 – 939
    Beta strandi97 – 1015
    Helixi104 – 1107
    Beta strandi118 – 1236
    Helixi127 – 13711
    Helixi142 – 15514
    Helixi156 – 1605
    Turni162 – 1643
    Beta strandi166 – 1705
    Helixi174 – 18411
    Helixi186 – 1916

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LVGX-ray2.10A1-198[»]
    ProteinModelPortaliQ64520.
    SMRiQ64520. Positions 5-194.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ64520.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 186183Guanylate kinase-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the guanylate kinase family.Curated
    Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0194.
    HOVERGENiHBG003344.
    InParanoidiQ64520.
    KOiK00942.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    InterProiIPR008145. GK/Ca_channel_bsu.
    IPR008144. Guanylate_kin-like.
    IPR017665. Guanylate_kinase.
    IPR020590. Guanylate_kinase_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00625. Guanylate_kin. 1 hit.
    [Graphical view]
    SMARTiSM00072. GuKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR03263. guanyl_kin. 1 hit.
    PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
    PS50052. GUANYLATE_KINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q64520-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGPRPVVLS GPSGAGKSTL LKKLFQEHSS IFGFSVSHTT RNPRPGEEDG    50
    KDYYFVTREM MQRDIAAGDF IEHAEFSGNL YGTSKEAVRA VQAMNRICVL 100
    DVDLQGVRSI KKTDLCPIYI FVQPPSLDVL EQRLRLRNTE TEESLAKRLA 150
    AARTDMESSK EPGLFDLVII NDDLDKAYAT LKQALSEEIK KAQGTGHA 198
    Length:198
    Mass (Da):21,918
    Last modified:January 23, 2007 - v2
    Checksum:iF584E4B6521C607B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53514 mRNA. Translation: AAC52652.1.
    BC024625 mRNA. Translation: AAH24625.1.
    RefSeqiXP_006532308.1. XM_006532245.1.
    XP_006532309.1. XM_006532246.1.
    XP_006532310.1. XM_006532247.1.
    UniGeneiMm.3624.

    Genome annotation databases

    GeneIDi14923.
    KEGGimmu:14923.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53514 mRNA. Translation: AAC52652.1 .
    BC024625 mRNA. Translation: AAH24625.1 .
    RefSeqi XP_006532308.1. XM_006532245.1.
    XP_006532309.1. XM_006532246.1.
    XP_006532310.1. XM_006532247.1.
    UniGenei Mm.3624.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LVG X-ray 2.10 A 1-198 [» ]
    ProteinModelPortali Q64520.
    SMRi Q64520. Positions 5-194.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q64520. 2 interactions.
    MINTi MINT-4099756.

    PTM databases

    PhosphoSitei Q64520.

    Proteomic databases

    PaxDbi Q64520.
    PRIDEi Q64520.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 14923.
    KEGGi mmu:14923.

    Organism-specific databases

    CTDi 2987.
    MGIi MGI:95871. Guk1.

    Phylogenomic databases

    eggNOGi COG0194.
    HOVERGENi HBG003344.
    InParanoidi Q64520.
    KOi K00942.

    Enzyme and pathway databases

    Reactomei REACT_196553. Abacavir metabolism.

    Miscellaneous databases

    ChiTaRSi GUK1. mouse.
    EvolutionaryTracei Q64520.
    PROi Q64520.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q64520.
    Bgeei Q64520.
    CleanExi MM_GUK1.
    Genevestigatori Q64520.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 hits.
    InterProi IPR008145. GK/Ca_channel_bsu.
    IPR008144. Guanylate_kin-like.
    IPR017665. Guanylate_kinase.
    IPR020590. Guanylate_kinase_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00625. Guanylate_kin. 1 hit.
    [Graphical view ]
    SMARTi SM00072. GuKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR03263. guanyl_kin. 1 hit.
    PROSITEi PS00856. GUANYLATE_KINASE_1. 1 hit.
    PS50052. GUANYLATE_KINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, characterization, and modeling of mouse and human guanylate kinases."
      Brady W.A., Kokoris M.S., Fitzgibbon M., Black M.E.
      J. Biol. Chem. 271:16734-16740(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Mammary gland.
    3. "Structural characterization of the closed conformation of mouse guanylate kinase."
      Sekulic N., Shuvalova L., Spangenberg O., Konrad M., Lavie A.
      J. Biol. Chem. 277:30236-30243(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), ATP-BINDING SITES, ACTIVE SITE.

    Entry informationi

    Entry nameiKGUA_MOUSE
    AccessioniPrimary (citable) accession number: Q64520
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3